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Conserved domains on  [gi|1489866108|ref|NP_001353587|]
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phospholipid-transporting ATPase VB isoform 5 [Homo sapiens]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 40-427 0e+00

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd02073:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 836  Bit Score: 577.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  40 GNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDLRRYKSDKVI 119
Cdd:cd02073     1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 120 NNRECLIYSRKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 199
Cdd:cd02073    81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 200 QFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 279
Cdd:cd02073   159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 280 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 359
Cdd:cd02073   239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866108 360 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEY 427
Cdd:cd02073   316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY 383
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 401-467 9.19e-04

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd01431:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 319  Bit Score: 41.28  E-value: 9.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866108 401 YIFSDKTGTLTENKMVFRRC-----------TIMGSEYSHQENGIEAPKGSIPLSKRKYPALLRNEEIKDILLALLEA 467
Cdd:cd01431     1 VICSDKTGTLTKNGMTVTKLfieeipfnstrKRMSVVVRLPGRYRAIVKGAPETILSRCSHALTEEDRNKIEKAQEES 78
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
 40-427 0e+00

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319770 [Multi-domain]  Cd Length: 836  Bit Score: 577.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  40 GNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDLRRYKSDKVI 119
Cdd:cd02073     1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 120 NNRECLIYSRKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 199
Cdd:cd02073    81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 200 QFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 279
Cdd:cd02073   159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 280 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 359
Cdd:cd02073   239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866108 360 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEY 427
Cdd:cd02073   316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY 383
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
 39-436 5.70e-145

phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes.


Pssm-ID: 273734 [Multi-domain]  Cd Length: 1057  Bit Score: 442.21  E-value: 5.70e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108   39 RGNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDLRRYKSDKV 118
Cdd:TIGR01652    2 CSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDKE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  119 INNRECLIYsRKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQE 198
Cdd:TIGR01652   82 VNNRLTEVL-EGHGQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRQALEETQKML 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  199 VQFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKR 278
Cdd:TIGR01652  161 DEDDIKNFSGEIECEQPNASLYSFQGNMTINGDRQYPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRNATQAPSKR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  279 SKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDanGSFLPSALGGFYMFLTMIILLQVLIPISLYVS 358
Cdd:TIGR01652  241 SRLEKELNFLIIILFCLLFVLCLISSVGAGIWNDAHGKDLWYIRLD--VSERNAAANGFFSFLTFLILFSSLIPISLYVS 318

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866108  359 IELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENGIEA 436
Cdd:TIGR01652  319 LELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDGFTEIKD 396
PLN03190 PLN03190
aminophospholipid translocase; Provisional
 31-428 8.97e-124

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 389.26  E-value: 8.97e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108   31 KENPNRHHRGNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDL 110
Cdd:PLN03190    80 KSNERFEFAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASILPLAFVLLVTAVKDAYEDW 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  111 RRYKSDKVINNRECLIYSRKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRcv 190
Cdd:PLN03190   160 RRHRSDRIENNRLAWVLVDDQ--FQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAYVQTINLDGESNLKTR-- 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  191 vkgFSQQEVQF---EPELFHNTIVCEKPNNHLNKFKGYMEhPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKA 267
Cdd:PLN03190   236 ---YAKQETLSkipEKEKINGLIKCEKPNRNIYGFQANME-VDGKRLSLGPSNIILRGCELKNTAWAIGVAVYCGRETKA 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  268 MLNNSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGT---------FEEHPPFDVPDA-NGSFLPSALGGF 337
Cdd:PLN03190   312 MLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRRhrdeldtipFYRRKDFSEGGPkNYNYYGWGWEIF 391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  338 YMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVF 417
Cdd:PLN03190   392 FTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTLTENKMEF 471

                          410
                   ....*....|.
gi 1489866108  418 RRCTIMGSEYS 428
Cdd:PLN03190   472 QCASIWGVDYS 482
PhoLip_ATPase_N pfam16209
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ...
 29-91 1.50e-19

Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes.


Pssm-ID: 465069 [Multi-domain]  Cd Length: 67  Bit Score: 82.52  E-value: 1.50e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489866108  29 SHKENPNRHHRGNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSM 91
Cdd:pfam16209   5 DPEKNSEFKYPSNKISTSKYTLLTFLPKNLFEQFRRVANLYFLLIAILQLIPGISPTGPYTTI 67
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
388-428 4.29e-06

Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 49.33  E-value: 4.29e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1489866108 388 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYS 428
Cdd:COG0474   312 RRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTYE 352
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 401-467 9.19e-04

ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 41.28  E-value: 9.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866108 401 YIFSDKTGTLTENKMVFRRC-----------TIMGSEYSHQENGIEAPKGSIPLSKRKYPALLRNEEIKDILLALLEA 467
Cdd:cd01431     1 VICSDKTGTLTKNGMTVTKLfieeipfnstrKRMSVVVRLPGRYRAIVKGAPETILSRCSHALTEEDRNKIEKAQEES 78
 
Name Accession Description Interval E-value
P-type_ATPase_APLT_Dnf-like cd02073
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
 40-427 0e+00

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319770 [Multi-domain]  Cd Length: 836  Bit Score: 577.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  40 GNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDLRRYKSDKVI 119
Cdd:cd02073     1 DNRISTTKYTVFTFLPKNLFEQFRRVANLYFLFIAILQQIPGISPTGPYTTLLPLLFVLGVTAIKEGYEDIRRHKSDNEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 120 NNRECLIYSRKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEV 199
Cdd:cd02073    81 NNRPVQVLRGGK--FVKKKWKDIRVGDIVRVKNDEFVPADLLLLSSSEPDGLCYVETANLDGETNLKIRQALPETALLLS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 200 QFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRS 279
Cdd:cd02073   159 EEDLARFSGEIECEQPNNDLYTFNGTLELNGGRELPLSPDNLLLRGCTLRNTEWVYGVVVYTGHETKLMLNSGGTPLKRS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 280 KIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSflpSALGGFYMFLTMIILLQVLIPISLYVSI 359
Cdd:cd02073   239 SIEKKMNRFIIAIFCILIVMCLISAIGKGIWLSKHGRDLWYLLPKEERS---PALEFFFDFLTFIILYNNLIPISLYVTI 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866108 360 ELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEY 427
Cdd:cd02073   316 EVVKFLQSFFINWDLDMYDEETDTPAEARTSNLNEELGQVEYIFSDKTGTLTENIMEFKKCSINGVDY 383
ATPase-Plipid TIGR01652
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ...
 39-436 5.70e-145

phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes.


Pssm-ID: 273734 [Multi-domain]  Cd Length: 1057  Bit Score: 442.21  E-value: 5.70e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108   39 RGNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDLRRYKSDKV 118
Cdd:TIGR01652    2 CSNKISTTKYTVLTFLPKNLFEQFKRFANLYFLVVALLQQVPILSPTYRGTSIVPLAFVLIVTAIKEAIEDIRRRRRDKE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  119 INNRECLIYsRKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQE 198
Cdd:TIGR01652   82 VNNRLTEVL-EGHGQFVEIPWKDLRVGDIVKVKKDERIPADLLLLSSSEPDGVCYVETANLDGETNLKLRQALEETQKML 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  199 VQFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKR 278
Cdd:TIGR01652  161 DEDDIKNFSGEIECEQPNASLYSFQGNMTINGDRQYPLSPDNILLRGCTLRNTDWVIGVVVYTGHDTKLMRNATQAPSKR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  279 SKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDanGSFLPSALGGFYMFLTMIILLQVLIPISLYVS 358
Cdd:TIGR01652  241 SRLEKELNFLIIILFCLLFVLCLISSVGAGIWNDAHGKDLWYIRLD--VSERNAAANGFFSFLTFLILFSSLIPISLYVS 318

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866108  359 IELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENGIEA 436
Cdd:TIGR01652  319 LELVKSVQAYFINSDLQMYHEKTDTPASVRTSNLNEELGQVEYIFSDKTGTLTQNIMEFKKCSIAGVSYGDGFTEIKD 396
PLN03190 PLN03190
aminophospholipid translocase; Provisional
 31-428 8.97e-124

aminophospholipid translocase; Provisional


Pssm-ID: 215623 [Multi-domain]  Cd Length: 1178  Bit Score: 389.26  E-value: 8.97e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108   31 KENPNRHHRGNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDL 110
Cdd:PLN03190    80 KSNERFEFAGNSIRTAKYSVFSFLPRNLFEQFHRVAYIYFLVIAVLNQLPQLAVFGRGASILPLAFVLLVTAVKDAYEDW 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  111 RRYKSDKVINNRECLIYSRKEqtYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRcv 190
Cdd:PLN03190   160 RRHRSDRIENNRLAWVLVDDQ--FQEKKWKDIRVGEIIKIQANDTLPCDMVLLSTSDPTGVAYVQTINLDGESNLKTR-- 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  191 vkgFSQQEVQF---EPELFHNTIVCEKPNNHLNKFKGYMEhPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKA 267
Cdd:PLN03190   236 ---YAKQETLSkipEKEKINGLIKCEKPNRNIYGFQANME-VDGKRLSLGPSNIILRGCELKNTAWAIGVAVYCGRETKA 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  268 MLNNSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGT---------FEEHPPFDVPDA-NGSFLPSALGGF 337
Cdd:PLN03190   312 MLNNSGAPSKRSRLETRMNLEIIILSLFLIALCTIVSVCAAVWLRRhrdeldtipFYRRKDFSEGGPkNYNYYGWGWEIF 391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  338 YMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVF 417
Cdd:PLN03190   392 FTFLMSVIVFQIMIPISLYISMELVRVGQAYFMIRDDQMYDEASNSRFQCRALNINEDLGQIKYVFSDKTGTLTENKMEF 471

                          410
                   ....*....|.
gi 1489866108  418 RRCTIMGSEYS 428
Cdd:PLN03190   472 QCASIWGVDYS 482
P-type_ATPase_APLT cd07536
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ...
 41-431 2.42e-104

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, Neo1p, and human ATP8A2, -9B, -10D, -11B, and -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. Mammalian ATP11C may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. The yeast Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Human putative ATPase phospholipid transporting 9B, ATP9B, localizes to the trans-golgi network in a CDC50 protein-independent manner. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319838 [Multi-domain]  Cd Length: 805  Bit Score: 329.95  E-value: 2.42e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  41 NQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDLRRYKSDKVIN 120
Cdd:cd07536     2 NSISNQKYNVFTFLPGVLYEQFKRFLNLYFLVIACLQFVPALKPGYLYTTWAPLIFILAVTMTKEAIDDFRRFQRDKEVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 121 NREclIYSRKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVkgfsqQEVQ 200
Cdd:cd07536    82 KKQ--LYSKLTGRKVQIKSSDIQVGDIVIVEKNQRIPSDMVLLRTSEPQGSCYVETAQLDGETDLKLRVAV-----SCTQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 201 FEPELFH-----NTIVCEKPNNHLNKFKGYM--EHPD-QTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNS 272
Cdd:cd07536   155 QLPALGDlmkisAYVECQKPQMDIHSFEGNFtlEDSDpPIHESLSIENTLLRASTLRNTGWVIGVVVYTGKETKLVMNTS 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 273 GPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFlpsalGGFYMFLTMIILLQVLIP 352
Cdd:cd07536   235 NAKNKVGLLDLELNRLTKALFLALVVLSLVMVTLQGFWGPWYGEKNWYIKKMDTTSD-----NFGRNLLRFLLLFSYIIP 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1489866108 353 ISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQE 431
Cdd:cd07536   310 ISLRVNLDMVKAVYAWFIMWDENMYYIGNDTGTVARTSTIPEELGQVVYLLTDKTGTLTQNEMIFKRCHIGGVSYGGQV 388
P-type_ATPase_APLT_Neo1-like cd07541
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ...
 41-419 2.16e-55

Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319841 [Multi-domain]  Cd Length: 792  Bit Score: 198.02  E-value: 2.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  41 NQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSMIPICVILAVTAIKDAWEDLRRYKSDKVIN 120
Cdd:cd07541     2 NEVRNQKYNIFTFLPKVLYEQFKFFYNLYFLVVALSQFVPALKIGYLYTYWAPLGFVLAVTMAKEAVDDIRRRRRDKEQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 121 NRECLIYSRKEQTYVqkcwKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVkGFSQQeVQ 200
Cdd:cd07541    82 YEKLTVRGETVEIPS----SDIKVGDLIIVEKNQRIPADMVLLRTSEKSGSCFIRTDQLDGETDWKLRIAV-PCTQK-LP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 201 FEPELFH-NTIVCEKPNNHLNKFKG-YMEHPDQTRTGFGCESLLLrGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKR 278
Cdd:cd07541   156 EEGILNSiSAVYAEAPQKDIHSFYGtFTINDDPTSESLSVENTLW-ANTVVASGTVIGVVVYTGKETRSVMNTSQPKNKV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 279 SKIERRMN--IDIFFC--IGILILMCLIGAVGHSiWngtfeehppfdvpdangsflpsalggfYMFLT-MIILLQVLIPI 353
Cdd:cd07541   235 GLLDLEINflTKILFCavLALSIVMVALQGFQGP-W---------------------------YIYLFrFLILFSSIIPI 286

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1489866108 354 SLYVSIELVKLGQVFFLSNDLDLydEETDLsiqcRALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 419
Cdd:cd07541   287 SLRVNLDMAKIVYSWQIEHDKNI--PGTVV----RTSTIPEELGRIEYLLSDKTGTLTQNEMVFKK 346
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 92-428 1.19e-46

ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.


Pssm-ID: 273656 [Multi-domain]  Cd Length: 545  Bit Score: 170.19  E-value: 1.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  92 IPICVILAVTAIKDAWEDLRRYKSDKVINNRECLIYsRKEQTYVQKcwKDVRVGDFIQMKCNEIVPADILLLFSSdpngi 171
Cdd:TIGR01494   5 LVLLFVLLEVKQKLKAEDALRSLKDSLVNTATVLVL-RNGWKEISS--KDLVPGDVVLVKSGDTVPADGVLLSGS----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 172 CHLETASLDGETNLKQRCVVKGfsqqevqfepelfhntivCEKPNNHLNKFKGYMEHpdQTRTGFGCeslllrgctirNT 251
Cdd:TIGR01494  77 AFVDESSLTGESLPVLKTALPD------------------GDAVFAGTINFGGTLIV--KVTATGIL-----------TT 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 252 EMAVGIVIYAGHETKAMLNNsgpryKRSKIERrmniDIFFCIGILILMCLIGAVGHSIWNGTfeehppfdvpdangsflp 331
Cdd:TIGR01494 126 VGKIAVVVYTGFSTKTPLQS-----KADKFEN----FIFILFLLLLALAVFLLLPIGGWDGN------------------ 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 332 salGGFYMFLTMIILLQVLIPISLYVSIELVKLGQvfflsnDLDLYDEetdlSIQCRALNIAEDLGQIQYIFSDKTGTLT 411
Cdd:TIGR01494 179 ---SIYKAILRALAVLVIAIPCALPLAVSVALAVG------DARMAKK----GILVKNLNALEELGKVDVICFDKTGTLT 245

                         330
                  ....*....|....*..
gi 1489866108 412 ENKMVFRRCTIMGSEYS 428
Cdd:TIGR01494 246 TNKMTLQKVIIIGGVEE 262
PhoLip_ATPase_N pfam16209
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ...
 29-91 1.50e-19

Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes.


Pssm-ID: 465069 [Multi-domain]  Cd Length: 67  Bit Score: 82.52  E-value: 1.50e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1489866108  29 SHKENPNRHHRGNQIKTSKYTVLSFVPKNIFEQLHRFANLYFVGIAVLNFIPVVNAFQPEVSM 91
Cdd:pfam16209   5 DPEKNSEFKYPSNKISTSKYTLLTFLPKNLFEQFRRVANLYFLLIAILQLIPGISPTGPYTTI 67
ATPase-IIB_Ca TIGR01517
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ...
 91-462 3.37e-06

plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase responsible for translocating calcium ions across the plasma membrane of eukaryotes, out of the cell. In some organisms, this type of pump may also be found in vacuolar membranes. In humans and mice, at least, there are multiple isoforms of the PMCA pump with overlapping but not redundant functions. Accordingly, there are no human diseases linked to PMCA defects, although alterations of PMCA function do elicit physiological effects. The calcium P-type ATPases have been characterized as Type IIB based on a phylogenetic analysis which distinguishes this group from the Type IIA SERCA calcium pump. A separate analysis divides Type IIA into sub-types (SERCA and PMR1) which are represented by two corresponding models (TIGR01116 and TIGR01522). This model is well separated from those.


Pssm-ID: 273668 [Multi-domain]  Cd Length: 956  Bit Score: 49.78  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  91 MIPICVILAVTAIKD-----AWEDLRRYKSDKVI----NNRECLIYSRkeqtyvqkcwkDVRVGDFIQMKCNEIVPADIL 161
Cdd:TIGR01517 138 LVSVILVVLVTAVNDykkelQFRQLNREKSAQKIavirGGQEQQISIH-----------DIVVGDIVSLSTGDVVPADGV 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 162 LLFSSDpngiCHLETASLDGETNLKQRCVVKgfsqqevqfEPELFHNTIVCEkpnnhlnkfkgymehpdqtrtGFGcesl 241
Cdd:TIGR01517 207 FISGLS----LEIDESSITGESDPIKKGPVQ---------DPFLLSGTVVNE---------------------GSG---- 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 242 llrgctiRNTEMAVGIVIYAGhETKAMLNNSGPryKRSKIERRMN-----IDIFFCIG--ILILMCLIGAVGHSIWNGTF 314
Cdd:TIGR01517 249 -------RMLVTAVGVNSFGG-KLMMELRQAGE--EETPLQEKLSelaglIGKFGMGSavLLFLVLSLRYVFRIIRGDGR 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 315 EEHPPFDVPdangSFLPsalggfyMFLTMIILLQVLIP--ISLYVSIELVKLGQVFFLSNDLdlydeetdlsiqCRALNI 392
Cdd:TIGR01517 319 FEDTEEDAQ----TFLD-------HFIIAVTIVVVAVPegLPLAVTIALAYSMKKMMKDNNL------------VRHLAA 375

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 393 AEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQEngieapkgsiPLSKRKYPALLRNEEIKDILL 462
Cdd:TIGR01517 376 CETMGSATAICSDKTGTLTQNVMSVVQGYIGEQRFNVRD----------EIVLRNLPAAVRNILVEGISL 435
MgtA COG0474
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];
388-428 4.29e-06

Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism];


Pssm-ID: 440242 [Multi-domain]  Cd Length: 874  Bit Score: 49.33  E-value: 4.29e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1489866108 388 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYS 428
Cdd:COG0474   312 RRLPAVETLGSVTVICTDKTGTLTQNKMTVERVYTGGGTYE 352
P-type_ATPase_Ca_prok cd02089
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ...
 388-447 5.60e-05

prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL and Listeria monocytogenes LMCA1; Ca(2+) transport ATPase is a plasma membrane protein which pumps Ca(2+) ion out of the cytoplasm. This prokaryotic subfamily includes the Ca(2+)-ATPase Synechococcus elongatus PacL, Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1) which has a low Ca(2+) affinity and a high pH optimum (pH about 9) and may remove Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH, and the Bacillus subtilis putative P-type Ca(2+)-transport ATPase encoded by the yloB gene, which is expressed during sporulation. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319781 [Multi-domain]  Cd Length: 674  Bit Score: 45.68  E-value: 5.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1489866108 388 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRR-CTI----------MGSEYSHQENGIEA--PK-GSIPL-SKRK 447
Cdd:cd02089   288 RKLPAVETLGSVSVICSDKTGTLTQNKMTVEKiYTIgdptetalirAARKAGLDKEELEKkyPRiAEIPFdSERK 362
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 401-467 9.19e-04

ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 41.28  E-value: 9.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1489866108 401 YIFSDKTGTLTENKMVFRRC-----------TIMGSEYSHQENGIEAPKGSIPLSKRKYPALLRNEEIKDILLALLEA 467
Cdd:cd01431     1 VICSDKTGTLTKNGMTVTKLfieeipfnstrKRMSVVVRLPGRYRAIVKGAPETILSRCSHALTEEDRNKIEKAQEES 78
P-type_ATPase_Na_ENA cd02086
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ...
 388-419 1.18e-03

fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces cerevisiae Ena1p, Ena2p and Ustilago maydis Ena1, and the endoplasmic reticulum sodium transporter Ustilago maydis Ena2; Fungal-type Na(+)-ATPase (also called ENA ATPases). This subfamily includes the Saccharomyces cerevisiae plasma membrane transporters: Na(+)/Li(+)-exporting ATPase Ena1p which may also extrudes K(+), and Na(+)-exporting P-type ATPase Ena2p. It also includes Ustilago maydis plasma membrane Ena1, an K(+)/Na(+)-ATPase whose chief role is to pump Na(+) and K(+) out of the cytoplasm, especially at high pH values, and endoplasmic reticulum Ena2 ATPase which mediates Na(+) or K(+) fluxes in the ER or in other endomembranes. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319780 [Multi-domain]  Cd Length: 920  Bit Score: 41.67  E-value: 1.18e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1489866108 388 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 419
Cdd:cd02086   317 RKLDALEALGAVTDICSDKTGTLTQGKMVVRQ 348
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
 388-415 1.75e-03

uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319840 [Multi-domain]  Cd Length: 634  Bit Score: 40.86  E-value: 1.75e-03
                          10        20
                  ....*....|....*....|....*...
gi 1489866108 388 RALNIAEDLGQIQYIFSDKTGTLTENKM 415
Cdd:cd07539   288 RSPRTVEALGRVDTICFDKTGTLTENRL 315
P-type_ATPase_cation cd02082
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ...
 92-418 1.85e-03

P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins and Saccharomyces cerevisiae Ypk9p and Spf1p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Saccharomyces 1 Spf1p may mediate manganese transport into the endoplasmic reticulum. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319777 [Multi-domain]  Cd Length: 786  Bit Score: 41.04  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  92 IPICVILAVTAIKDAWEDLRRYKSDKVI-NNRECLIYSRKEQTYVQKCWKDVRVGDFIQMKCNE-IVPADILLLfssdpN 169
Cdd:cd02082    54 ITVVFMTTINSLSCIYIRGVMQKELKDAcLNNTSVIVQRHGYQEITIASNMIVPGDIVLIKRREvTLPCDCVLL-----E 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 170 GICHLETASLDGETNLKQRCVVKGFSQQEVQFEPE------LFHNTIVcekpnnhlnkfkgyMEHpdQTRTGFGCESLLL 243
Cdd:cd02082   129 GSCIVTEAMLTGESVPIGKCQIPTDSHDDVLFKYEsskshtLFQGTQV--------------MQI--IPPEDDILKAIVV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 244 RgctirntemaVGIVIYAGHETKAMLnnsgprYKRsKIERRMNIDIFFCIGILILMCLIGAVgHSIWNGTFEEHPPfdvp 323
Cdd:cd02082   193 R----------TGFGTSKGQLIRAIL------YPK-PFNKKFQQQAVKFTLLLATLALIGFL-YTLIRLLDIELPP---- 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 324 dangsflpsalgGFYMFLTMIILLQVLIP-----ISLYVSIELVKLGQvfflsndldlydeetdLSIQCRALNIAEDLGQ 398
Cdd:cd02082   251 ------------LFIAFEFLDILTYSVPPglpmlIAITNFVGLKRLKK----------------NQILCQDPNRISQAGR 302

                         330       340
                  ....*....|....*....|
gi 1489866108 399 IQYIFSDKTGTLTENKMVFR 418
Cdd:cd02082   303 IQTLCFDKTGTLTEDKLDLI 322
P-type_ATPase_cation cd02080
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ...
 388-419 2.26e-03

P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase; This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319775 [Multi-domain]  Cd Length: 819  Bit Score: 40.71  E-value: 2.26e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1489866108 388 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRR 419
Cdd:cd02080   288 RRLPAVETLGSVTVICSDKTGTLTRNEMTVQA 319
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
 388-451 2.50e-03

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319778 [Multi-domain]  Cd Length: 979  Bit Score: 40.74  E-value: 2.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1489866108 388 RALNIAEDLGQIQYIFSDKTGTLTENKM-VFRRCTIMGSEYSHQENGIE------APKGSIPLSKRK-----YPAL 451
Cdd:cd02083   329 RSLPSVETLGCTSVICSDKTGTLTTNQMsVSRMFILDKVEDDSSLNEFEvtgstyAPEGEVFKNGKKvkagqYDGL 404
P-type_ATPase_Ca_PMCA-like cd02081
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ...
 94-422 3.23e-03

animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related Ca2(+)-ATPases including Saccharomyces cerevisiae vacuolar PMC1; Animal PMCAs function to export Ca(2+) from cells and play a role in regulating Ca(2+) signals following stimulus induction and in preventing calcium toxicity. Many PMCA pump variants exist due to alternative splicing of transcripts. PMCAs are regulated by the binding of calmodulin or by kinase-mediated phosphorylation. Saccharomyces cerevisiae vacuolar transporter Pmc1p facilitates the accumulation of Ca2+ into vacuoles. Pmc1p is not regulated by direct calmodulin binding but responds to the calmodulin/calcineurin-signaling pathway and is controlled by the transcription factor complex Tcn1p/Crz1p. Similarly, the expression of the gene for Dictyostelium discoideum Ca(2+)-ATPase PAT1, patA, is under the control of a calcineurin-dependent transcription factor. Plant vacuolar Ca(2+)-ATPases, are regulated by direct-calmodulin binding. Plant Ca(2+)-ATPases are present at various cellular locations including the plasma membrane, endoplasmic reticulum, chloroplast and vacuole. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319776 [Multi-domain]  Cd Length: 721  Bit Score: 40.26  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108  94 ICVILaVTAIKDAWEDLRRYKSDKVINNRECLIYSRKEQTYVQKcwKDVRVGDFIQMKCNEIVPADILLLFSSDpngiCH 173
Cdd:cd02081    73 ILVVL-VTAGNDYQKEKQFRKLNSKKEDQKVTVIRDGEVIQISV--FDIVVGDIVQLKYGDLIPADGLLIEGND----LK 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 174 LETASLDGETNlkqrcvvkgfsqqevqfepelfhntivcekpnnHLNKfKGYMEHPDqtrtgfgceSLLLRGCTIR--NT 251
Cdd:cd02081   146 IDESSLTGESD---------------------------------PIKK-TPDNQIPD---------PFLLSGTKVLegSG 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 252 EM---AVGIVIYAGhETKAMLNNSGPRykRSKIERRMN---IDI-FFCIGILILMcLIGAVGHSIWNGTFEEHPPFDVPD 324
Cdd:cd02081   183 KMlvtAVGVNSQTG-KIMTLLRAENEE--KTPLQEKLTklaVQIgKVGLIVAALT-FIVLIIRFIIDGFVNDGKSFSAED 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489866108 325 ANgSFLPSalggfymFLTMIILLQVLIP--------ISLYVSIelvklgQVFFLSNDLdlydeetdlsiqCRALNIAEDL 396
Cdd:cd02081   259 LQ-EFVNF-------FIIAVTIIVVAVPeglplavtLSLAYSV------KKMMKDNNL------------VRHLDACETM 312

                         330       340
                  ....*....|....*....|....*.
gi 1489866108 397 GQIQYIFSDKTGTLTENKMVFRRCTI 422
Cdd:cd02081   313 GNATAICSDKTGTLTQNRMTVVQGYI 338
P-type_ATPase_SPCA cd02085
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ...
 388-424 5.23e-03

golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319779 [Multi-domain]  Cd Length: 804  Bit Score: 39.69  E-value: 5.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1489866108 388 RALNIAEDLGQIQYIFSDKTGTLTENKM--------------VFRRCTIMG 424
Cdd:cd02085   280 KKLPIVETLGCVNVICSDKTGTLTKNEMtvtkivtgcvcnnaVIRNNTLMG 330
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
 394-420 6.97e-03

P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319774 [Multi-domain]  Cd Length: 617  Bit Score: 39.12  E-value: 6.97e-03
                          10        20
                  ....*....|....*....|....*..
gi 1489866108 394 EDLGQIQYIFSDKTGTLTENKMVFRRC 420
Cdd:cd02079   312 ETLAKVDTVAFDKTGTLTEGKPEVTEI 338
ATPase-IID_K-Na TIGR01523
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ...
 388-422 9.45e-03

potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium efflux ATPase, more recent work has shown that the S. pombe CTA3 gene is in fact a potassium ion efflux pump. This model describes the clade of fungal P-type ATPases responsible for potassium and sodium efflux. The degree to which these pumps show preference for sodium or potassium varies. This group of ATPases has been classified by phylogentic analysis as type IID. The Leishmania sequence (GP|3192903), which falls between trusted and noise in this model, may very well turn out to be an active potassium pump.


Pssm-ID: 130586 [Multi-domain]  Cd Length: 1053  Bit Score: 38.84  E-value: 9.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1489866108  388 RALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTI 422
Cdd:TIGR01523  348 RKLDALEALGAVNDICSDKTGTITQGKMIARQIWI 382
P-type_ATPase_H cd02076
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ...
 394-430 9.64e-03

plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+)-ATPases; This subfamily includes eukaryotic plasma membrane H(+)-ATPase which transports H(+) from the cytosol to the extracellular space, thus energizing the plasma membrane for the uptake of ions and nutrients, and is expressed in plants and fungi. This H(+)-ATPase consists of four domains: a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. This subfamily also includes the putative P-type H(+)-ATPase, MJ1226p of the anaerobic hyperthermophilic archaea Methanococcus jannaschii. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319771 [Multi-domain]  Cd Length: 781  Bit Score: 38.75  E-value: 9.64e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1489866108 394 EDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQ 430
Cdd:cd02076   279 EELAGVDILCSDKTGTLTLNKLSLDEPYSLEGDGKDE 315
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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